[Kraev A] Originally identified by similarity to mammalian PMCA family proteins in Genome Project data, mca-1 was expressed in insect cells and shown to have the predicted activity: aspartyl-phosphate formation in the presence of calcium, like mammalian counterparts, has a calmodulin-binding domain at the C-terminus and actually binds human calmodulin in a standard assay. Two other related sequences identified in the genomic sequencing data "in progress" and cDNAs finished by direct RT-PCR product sequencing. Mca-3 shows the highest sequence similarity to the mammalian analogues (77% on aminoacid). All three mca sequences have calmodulin-binding domains at the same location as their mammalian counterparts and the same predicted trans-membrane topology
mca-1 encodes one of three C. elegans plasma membrane Ca2+ ATPases (PMCAs); by homology, MCA-1 is predicted to function as a molecular pump that couples ATP hydrolysis to extrusion of cytosolic Ca2+; when expressed in insect cells, MCA-1 exhibits calcium-pumping ATPase activity and binding to human calmodulin; large-scale RNAi screens indicate that mca-1 activity is required for normal coordinated locomotion and rates of growth; an mca-1::gfp reporter fusion is expressed solely in the excretory canal.
Enables P-type calcium transporter activity and calmodulin binding activity. Involved in calcium ion transport and intracellular calcium ion homeostasis. Located in membrane. Expressed in excretory canal.
Map position created from combination of previous interpolated map position (based on known location of sequence) and allele information. Therefore this is not a genetic map position based on recombination frequencies or genetic experiments. This was done on advice of the CGC.